Abstract:
:The physical and catalytic properties of 5 histidine-serine mutants of human 5-lipoxygenase (5-LO) have been characterized. The mutants HS363, HS391 and HS400 have activities, pH optima and stabilities similar to those of the wild type enzyme. The iron content of each of these mutants is 0.30-0.53 mol Fe/mol 5-LO which is within the range observed for the wild type enzyme. HS368 contains iron (0.15 and 0.43 mol Fe/mol 5-LO in 2 preparations) but has no detectable oxygenase, leukotriene A4 synthase or anaerobic arachidonate-dependent hydroperoxidase activities. HS368 does have significant reducing agent-dependent hydroperoxidase activity suggesting that His-368 may not be an iron ligand but rather may be involved in interactions with arachidonic acid or the formation of the arachidonyl radical intermediate. HS373 contains no iron and has no detectable activities.
journal_name
Biochem Biophys Res Communjournal_title
Biochemical and biophysical research communicationsauthors
Percival MD,Ouellet Mdoi
10.1016/s0006-291x(05)81542-6subject
Has Abstractpub_date
1992-08-14 00:00:00pages
1265-70issue
3eissn
0006-291Xissn
1090-2104pii
S0006-291X(05)81542-6journal_volume
186pub_type
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